Phospholipase C From Alternaria alternata Is Induced by Physiochemical Cues on the Pear Fruit Surface That Dictate Infection Structure Differentiation and Pathogenicity

Huang, Yi; Li, Dongmei; Bi, Yang; Prusky, Dov; Yupeng, Dong; Wang, Tiaolan; Zhang, Miao; Zhang, Xuemei; Liu, Yongxiang

doi:10.3389/fmicb.2020.01279

Cited by 20 publications

(13 citation statements)

References 68 publications

(87 reference statements)

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“…The PH domain is localized at the N-terminus of PLCs and is responsible for membrane PtdIns(4,5)P 2 binding [ 67 ]. PLCs, such as those from PLC1 from Alternaria alternata [ 68 ] and Magnaporthe oryzae [ 69 ], encode a PH domain, which is in tandem with the EF-hand Ca 2+ -binding, the catalytic X and Y, and the phospholipid-binding C2 domains. Regulation of phospholipid-binding of PLC is mediated by association of PtdIns4P 5-kinase and Ca 2+ to the PH and C2 domains, respectively [ 70 ].…”

Section: Resultsmentioning

confidence: 99%

The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals

Hasan

Capelluto

2022

Membranes

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Phafin2, a member of the Phafin family of proteins, contributes to a plethora of cellular activities including autophagy, endosomal cargo transportation, and macropinocytosis. The PH and FYVE domains of Phafin2 play key roles in membrane binding, whereas the C-terminal poly aspartic acid (polyD) motif specifically autoinhibits the PH domain binding to the membrane phosphatidylinositol 3-phosphate (PtdIns3P). Since the Phafin2 FYVE domain also binds PtdIns3P, the role of the polyD motif remains unclear. In this study, bioinformatics tools and resources were employed to determine the concurrence of the PH-FYVE module with the polyD motif among Phafin2 and PH-, FYVE-, or polyD-containing proteins from bacteria to humans. FYVE was found to be an ancient domain of Phafin2 and is related to proteins that are present in both prokaryotes and eukaryotes. Interestingly, the polyD motif only evolved in Phafin2 and PH- or both PH-FYVE-containing proteins in animals. PolyD motifs are absent in PH domain-free FYVE-containing proteins, which usually display cellular trafficking or autophagic functions. Moreover, the prediction of the Phafin2-interacting network indicates that Phafin2 primarily cross-talks with proteins involved in autophagy, protein trafficking, and neuronal function. Taken together, the concurrence of the polyD motif with the PH domain may be associated with complex cellular functions that evolved specifically in animals.

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Section: Resultsmentioning

confidence: 99%

The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals

Hasan

Capelluto

2022

Membranes

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“…In order to precisely regulate intracellular calcium signals, organisms have also evolved several calcium-sensing proteins to respond to different ranges of Ca 2+ concentration levels [ 70 ]. CaM, located downstream of phospholipase C [ 71 ] in the calcium signaling pathway, is a very important Ca 2+ sensor that can sense the change of intracellular Ca 2+ concentration and regulate a series of downstream target proteins by binding with Ca 2+ [ 72 , 73 , 74 ]. CaN, as a Ca 2+ and CaM dependent serine/threonine protein phosphatase, is composed of the catalytic subunit CNA and the regulatory subunit CNB [ 75 , 76 , 77 , 78 , 79 ], and is the central mediator of the Ca 2+ /calmodulin/calcineurin/Crz1 signaling pathway.…”

Section: Calcium Signaling Pathway In Fungal Cellmentioning

confidence: 99%

Updating Insights into the Regulatory Mechanisms of Calcineurin-Activated Transcription Factor Crz1 in Pathogenic Fungi

Yang

Xie

et al. 2022

JoF

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Ca2+, as a second messenger in cells, enables organisms to adapt to different environmental stresses by rapidly sensing and responding to external stimuli. In recent years, the Ca2+ mediated calcium signaling pathway has been studied systematically in various mammals and fungi, indicating that the pathway is conserved among organisms. The pathway consists mainly of complex Ca2+ channel proteins, calcium pumps, Ca2+ transporters and many related proteins. Crz1, a transcription factor downstream of the calcium signaling pathway, participates in regulating cell survival, ion homeostasis, infection structure development, cell wall integrity and virulence. This review briefly summarizes the Ca2+ mediated calcium signaling pathway and regulatory roles in plant pathogenic fungi. Based on discussing the structure and localization of transcription factor Crz1, we focus on the regulatory role of Crz1 on growth and development, stress response, pathogenicity of pathogenic fungi and its regulatory mechanisms. Furthermore, we explore the cross-talk between Crz1 and other signaling pathways. Combined with the important role and pathogenic mechanism of Crz1 in fungi, the new strategies in which Crz1 may be used as a target to explore disease control in practice are also discussed.

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“…PDA media were added with TFP at the final concentrations of 10 μmol l −1 , inoculated with mycelium of A.alternata and cultured in an incubator at 28°C for 5 days, and ~0.25/0.5 g of the mycelium was sampled for melanin and toxin extracting, respectively. The extraction and determination of melanin and toxins were performed according to the method of Wang et al (2016) and Huang et al (2020). All the experiments were repeated at least three times.…”

Section: Melanin and Toxins Assaysmentioning

confidence: 99%

“…Although numerous studies have shown that CaM is involved in the regulation of fungal growth, secondary metabolism and pathogenicity, its regulatory role is diverse and complex depending on the pathogen. Our recent studies showed that protein kinase A (PKA) in the cAMP/ PKA pathway (Zhang et al, 2020), Sho1 in MAPK cascades (Liu et al, 2021) and PLC (Huang et al, 2020) in the Ca 2+ signalling pathway were involved in the vegetative growth, stress response and infection structure differentiation of A. alternata in response to hydrophobic and pear wax. At the same time, the importance of the Ca 2+ signalling pathway for infection structure differentiation of A. alternata was evaluated through the specific inhibitors of the Ca 2+ signalling pathway.…”

Section: Introductionmentioning

confidence: 99%

AaCaM is required for infection structure differentiation and secondary metabolites in pear fungal pathogen Alternaria alternata

Jiang

Mao

et al. 2022

Journal of Applied Microbiology

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Aims Calmodulin (CaM), acts as a kind of multifunctional Ca2+ sensing protein, which is ubiquitous in fungi, is highly conserved across eukaryotes and is involved in the regulation of a range of physiological processes, including morphogenesis, reproduction and secondary metabolites biosynthesis. Our aim was to understand the characteristics and functions of AaCaM in Alternaria alternata, the causal agent of pear black spot. Methods and results A 450 bp cDNA sequence of AaCaM gene of A. alternata was cloned by the PCR homology method. Sequence analysis showed that this protein encoded by AaCaM was a stable hydrophilic protein and had a high similarity to Neurospora crassa (CAA50271.1) and other fungi. RT‐qPCR analysis determined that AaCaM was differentially upregulated during infection structural differentiation of A. alternata both on hydrophobic and pear wax extract‐coated surface, with a 3.37‐fold upregulation during the hydrophobic induced appressorium formation period (6 h) and a 1.46‐fold upregulation during the infection hyphae formation period (8 h) following pear wax induction. Pharmaceutical analysis showed that the CaM‐specific inhibitor, trifluoperazine (TFP), inhibited spore germination and appressorium formation, and affected toxins and melanin biosynthesis in A. alternata. Conclusions AaCaM plays an important role in regulating infection structure differentiation and secondary metabolism of A. alternata. Significance and impact of study Our study provides a theoretical basis for further in‐depth investigation of the specific role of AaCaM in the calcium signalling pathway underlying hydrophobic and pear wax‐induced infection structure differentiation and pathogenicity of A. alternata.

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Phospholipase C From Alternaria alternata Is Induced by Physiochemical Cues on the Pear Fruit Surface That Dictate Infection Structure Differentiation and Pathogenicity

Cited by 20 publications

References 68 publications

The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals

The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals

Updating Insights into the Regulatory Mechanisms of Calcineurin-Activated Transcription Factor Crz1 in Pathogenic Fungi

AaCaM is required for infection structure differentiation and secondary metabolites in pear fungal pathogen Alternaria alternata

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